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Genetic screening coupled with gene-editing protein function testing is an effective and reliable method by which causative gene mutations of MODY can be identified.
The correlation suggests that RNA editing affects protein functions indirectly by regulating protein stability as well as sometimes being essential for protein enzymatic activity.
Mutational analyses of edited codons have demonstrated that editing is essential for protein function in vivo [ 4, 5].
Finally, to validate variants of one of the genes of interest (glucokinase, GCK) as pathogenic mutations, protein function editing by the variant genes was assessed.
However, although closely related, not every C T difference between M. polymorpha and P. endiviifolia coding regions reflects an actual editing site because only sites that are important for protein function seem to undergo editing.
Genome editing can be used to study protein function by altering coding sequence or achieve transcriptional control by altering the sequence of regulatory regions.
By contrast, the rather minor physico-chemical change provided by an H-to-Y amino acid transition mediated by matK-2 editing might be less critical for protein function.
Unlike alternative splicing, which shuffles relatively large regions of RNA, editing targets single bases in order to fine-tune protein function.
The MatK protein may tolerate both amino acids, in which case the loss of RNA editing would have only limited consequences for protein function.
The post-transcriptional sequence modification of transcripts through RNA editing is an important mechanism for regulating protein function and is associated with human disease phenotypes.
Post-transcriptional sequence modification of transcripts through RNA editing is also an important mechanism for regulating protein function and is associated with many human diseases.
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